MALT1_HUMAN - dbPTM
MALT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MALT1_HUMAN
UniProt AC Q9UDY8
Protein Name Mucosa-associated lymphoid tissue lymphoma translocation protein 1
Gene Name MALT1
Organism Homo sapiens (Human).
Sequence Length 824
Subcellular Localization Cytoplasm, perinuclear region . Nucleus . Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10.
Protein Description Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity. MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion. Involved in the induction of T helper 17 cells (Th17) differentiation. Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (By similarity)..
Protein Sequence MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMPGSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTEDELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRALTDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLDIDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRGLGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSRSNVPVETTDEIPFSFSDRLRISEK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSLLGDPLQ
------CCCCCCCCC		32.0924719451
2Acetylation------MSLLGDPLQ
------CCCCCCCCC		32.0922814378
18PhosphorylationLPPSAAPTGPLLAPP
CCCCCCCCCCCCCCC		46.86-
29PhosphorylationLAPPAGATLNRLREP
CCCCCCHHHHHHHHH		24.53-
42PhosphorylationEPLLRRLSELLDQAP
HHHHHHHHHHHHHCC		25.1228450419
63PhosphorylationRLAELAGSRGRLRLS
HHHHHHCCCCCEEEE		26.4222210691
70PhosphorylationSRGRLRLSCLDLEQC
CCCCEEEEEEEHHHC		13.2430108239
87PhosphorylationKVLEPEGSPSLCLLK
EEECCCCCHHHHHHH		15.0620860994
89PhosphorylationLEPEGSPSLCLLKLM
ECCCCCHHHHHHHHH		33.1520860994
94UbiquitinationSPSLCLLKLMGEKGC
CHHHHHHHHHCCCCC		24.39-
123PhosphorylationTEVLQLLSPPGIKIT
CHHHHHHCCCCCEEE		37.3325159151
130PhosphorylationSPPGIKITVNPESKA
CCCCCEEEECHHHHH		14.8226074081
135 (in isoform 2)Phosphorylation-27.46-
135PhosphorylationKITVNPESKAVLAGQ
EEEECHHHHHHHHHH		27.4630278072
136UbiquitinationITVNPESKAVLAGQF
EEECHHHHHHHHHHH		40.63-
253PhosphorylationLQCVAVGSPIPHYQW
EEEEECCCCCCCCHH		17.0422617229
272AcetylationLPLTHETKKLYMVPY
CCCCCCCEEEEEEEE		37.4825953088
272UbiquitinationLPLTHETKKLYMVPY
CCCCCCCEEEEEEEE		37.48-
331UbiquitinationNLGHPDNKEQTTDQP
HCCCCCCCCCCCCCC		59.59-
334O-linked_GlycosylationHPDNKEQTTDQPLAK
CCCCCCCCCCCCCHH		33.1723301498
341UbiquitinationTTDQPLAKDKVALLI
CCCCCCHHHHEEHEE		66.81-
387PhosphorylationVVSLLDLTEYEMRNA
EEEHHHCCHHHHHHH		35.87-
466UbiquitinationFLLDMCRKRNDYDDT
HHHHHHHHCCCCCCC		51.10-
470PhosphorylationMCRKRNDYDDTIPIL
HHHHCCCCCCCCHHH		21.1928796482
473PhosphorylationKRNDYDDTIPILDAL
HCCCCCCCCHHHHHH		26.2528796482
516UbiquitinationGIFMKFLKDRLLEDK
CHHHHHHHHHHCCCC		43.89-
538UbiquitinationEVAEDMGKCHLTKGK
HHHHHHCCCCCCCCH		16.31-
543UbiquitinationMGKCHLTKGKQALEI
HCCCCCCCCHHHHHH		71.16-
545UbiquitinationKCHLTKGKQALEIRS
CCCCCCCHHHHHHHH		33.67-
557UbiquitinationIRSSLSEKRALTDPI
HHHHHHHHCCCCCCC		39.33-
569PhosphorylationDPIQGTEYSAESLVR
CCCCCCCCCHHHHHH		17.0227642862
573PhosphorylationGTEYSAESLVRNLQW
CCCCCHHHHHHHHHH		31.70-
582UbiquitinationVRNLQWAKAHELPES
HHHHHHHHHCCCCHH		47.52-
637 (in isoform 2)Ubiquitination-11.7321906983
644UbiquitinationLDLDIDPKDANKGTP
CCCCCCHHHCCCCCC		66.77-
648 (in isoform 1)Ubiquitination-66.9221906983
648UbiquitinationIDPKDANKGTPEETG
CCHHHCCCCCCCCCC		66.922190698
660PhosphorylationETGSYLVSKDLPKHC
CCCCEEECCCCCHHH		20.18-
661UbiquitinationTGSYLVSKDLPKHCL
CCCEEECCCCCHHHH		56.67-
665UbiquitinationLVSKDLPKHCLYTRL
EECCCCCHHHHHHHH		55.00-
669PhosphorylationDLPKHCLYTRLSSLQ
CCCHHHHHHHHHHHH		8.6630576142
670PhosphorylationLPKHCLYTRLSSLQK
CCHHHHHHHHHHHHH		16.5230576142
674PhosphorylationCLYTRLSSLQKLKEH
HHHHHHHHHHHHHHH		39.1430576142
677UbiquitinationTRLSSLQKLKEHLVF
HHHHHHHHHHHHHHE		67.81-
679UbiquitinationLSSLQKLKEHLVFTV
HHHHHHHHHHHHEEE		50.56-
702UbiquitinationLEDTVEDKQEVNVGK
CCCCCCCHHHCCCCC		34.55-
709UbiquitinationKQEVNVGKPLIAKLD
HHHCCCCCCCEEHHH		32.16-
714UbiquitinationVGKPLIAKLDMHRGL
CCCCCEEHHHHCCCC		37.72-
724UbiquitinationMHRGLGRKTCFQTCL
HCCCCCCCHHHHHHH		48.09-
788PhosphorylationRTPDAFISSFAHHAS
CCCCHHHHHHHHHHH		16.9827080861
789PhosphorylationTPDAFISSFAHHASC
CCCHHHHHHHHHHHC		22.9527080861
795PhosphorylationSSFAHHASCHFSRSN
HHHHHHHHCCCCCCC		12.0828857561
799PhosphorylationHHASCHFSRSNVPVE
HHHHCCCCCCCCCCE		15.9028857561
824UbiquitinationDRLRISEK-------
HCCEECCC-------		59.87-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
573SPhosphorylationKinaseCK1AP48729
PSP
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:15125833
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:16775419
-KUbiquitinationE3 ubiquitin ligaseHECTD3Q5T447
PMID:23358872
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MALT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MALT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL10_HUMANBCL10physical
11090634
TRAF6_HUMANTRAF6physical
15125833
TRAF2_HUMANTRAF2physical
15125833
BCL10_HUMANBCL10physical
19279678
CSN5_HUMANCOPS5physical
19444310
KCC2G_HUMANCAMK2Gphysical
21513986
BCL10_HUMANBCL10physical
21513986
NEMO_HUMANIKBKGphysical
18931663
MALT1_HUMANMALT1physical
21966355
RELB_HUMANRELBphysical
21873235
MALT1_HUMANMALT1physical
22366302
MALT1_HUMANMALT1physical
11262391
BCL10_HUMANBCL10physical
18806265
TRAF2_HUMANTRAF2physical
19234489
TRAF6_HUMANTRAF6physical
19234489
DBLOH_HUMANDIABLOphysical
19234489
BCL10_HUMANBCL10physical
17189706
UBP2_HUMANUSP2physical
23264041
TRAF6_HUMANTRAF6physical
23264041
TAB2_HUMANTAB2physical
17948050
M3K7_HUMANMAP3K7physical
17948050
HECD3_HUMANHECTD3physical
23358872
SQSTM_HUMANSQSTM1physical
16874300
MALT1_HUMANMALT1physical
14695475
BCL10_HUMANBCL10physical
23690623
USP9X_HUMANUSP9Xphysical
23690623
KDM1A_HUMANKDM1Aphysical
23455924
CARM1_HUMANCARM1physical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
RNF31_HUMANRNF31physical
24491438
TNAP3_HUMANTNFAIP3physical
24491438
UB2V2_HUMANUBE2V2physical
14695475
UBE2N_HUMANUBE2Nphysical
14695475
CAR11_HUMANCARD11physical
25748427
BCL10_HUMANBCL10physical
25748427
NEMO_HUMANIKBKGphysical
25748427
M3K7_HUMANMAP3K7physical
25748427
TAB2_HUMANTAB2physical
25748427
BCL10_HUMANBCL10physical
25569716
TRAF6_HUMANTRAF6physical
25569716
HOIL1_HUMANRBCK1physical
26525107
KPCD_HUMANPRKCDphysical
22528498
TRAF6_HUMANTRAF6physical
22528498
BCL10_HUMANBCL10physical
19118383
KC1A_HUMANCSNK1A1physical
19118383
IKKB_HUMANIKBKBphysical
19118383
CAR14_HUMANCARD14physical
27113748
BCL10_HUMANBCL10physical
27113748
BCL10_HUMANBCL10physical
27071417
CAR14_HUMANCARD14physical
27071417
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615468Immunodeficiency 12 (IMD12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MALT1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory